Time-Resolved Fluorescence Spectroscopy is a powerful tool for biochemistry. Fluorometry can provide unique insights into the structure, assembly and flexibility of complex macromolecules. We continue to develop and exploit laser-based technology for such studies. This year, we completed and published the first phase of our studies into the Zn++- dependent activation and oligomerization of HIV-integrase, the enzyme used by the AIDS virus to integrate itself into protected sites within our own DNA. We employed a stopped-flow lifetime and anisotropy fluorometer of our own design to watch, e.g., the EDTA-induced dissociation of subunits. To begin the second phase, we also began to construct mutant proteins lacking certain tryptophan residues with the eventual goal of using many single tryptophan-bearing enzymes as structural reporter groups. We demonstated a new long range fluorescence resonance energy transfer mechanism (named "golden ruler") that uses the surface plasmon resonance absorbance of colloidal metals like gold to serve as ultrastrong (2,000,000 molar extinction) acceptors. This leads to effective ranges of 50-250+/-, some threefold greater than current methods. We also began collaborative studies into the molten globule states of multiple native, mutant and chemically modified apomyoglobins used as folding models, along with some model peptides, using DAS (decay associated spectra) to look for changes in tryptophan environments. We also completed and published fluorescent DNA-base analog studies, examined phosphors as potential cell thermometers, began testing our "Lumisonic" imaging media, and examined the flexibilty of DNA segments in contact with repressor proteins.